7etm
From Proteopedia
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<StructureSection load='7etm' size='340' side='right'caption='[[7etm]], [[Resolution|resolution]] 5.90Å' scene=''> | <StructureSection load='7etm' size='340' side='right'caption='[[7etm]], [[Resolution|resolution]] 5.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ETM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ETM FirstGlance]. <br> |
- | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7etm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7etm OCA], [https://pdbe.org/7etm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7etm RCSB], [https://www.ebi.ac.uk/pdbsum/7etm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7etm ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5.9Å</td></tr> |
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7etm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7etm OCA], [https://pdbe.org/7etm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7etm RCSB], [https://www.ebi.ac.uk/pdbsum/7etm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7etm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
- | == Function == | ||
- | [[https://www.uniprot.org/uniprot/Q6RXD3_HCMV Q6RXD3_HCMV]] Forms a portal in the viral capsid through which viral DNA is translocated during DNA packaging. Assembles as a dodecamer at a single fivefold axe of the T=16 icosahedric capsid. Binds to the molecular motor that translocates the viral DNA, termed terminase.[HAMAP-Rule:MF_04012] | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | How the human cytomegalovirus (HCMV) genome-the largest among human herpesviruses-is packaged, retained, and ejected remains unclear. We present the in situ structures of the symmetry-mismatched portal and the capsid vertex-specific components (CVSCs) of HCMV. The 5-fold symmetric 10-helix anchor-uncommon among known portals-contacts the portal-encircling DNA, which is presumed to squeeze the portal as the genome packaging proceeds. We surmise that the 10-helix anchor dampens this action to delay the portal reaching a "head-full" packaging state, thus facilitating the large genome to be packaged. The 6-fold symmetric turret, latched via a coiled coil to a helix from a major capsid protein, supports the portal to retain the packaged genome. CVSCs at the penton vertices-presumed to increase inner capsid pressure-display a low stoichiometry, which would aid genome retention. We also demonstrate that the portal and capsid undergo conformational changes to facilitate genome ejection after viral cell entry. | ||
- | + | ==See Also== | |
- | + | *[[Portal protein 3D structures|Portal protein 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Human cytomegalovirus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Li | + | [[Category: Li Z]] |
- | [[Category: Yu | + | [[Category: Yu X]] |
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Current revision
C6 portal vertex in the enveloped virion capsid
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